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Palmitoylated PSD95 is detected by immunocytochemistry using anti-PSD-95 (palmitoylated), mAb (rec.) (PF11) (Prod. No AG-27B-0021). Method: HeLa cells were cotransfected with DHHC2 (palmitoylating enzyme) + PSD95-GFP (A) or DHHC2 (palmitoylat

anti-PSD-95 (palmitoylated), mAb (rec.) (PF11) for ICC, IHC in Human, Mouse, Rat by AdipoGen Life Sciences. Order at Bio-Connect.

AG-27B-0021 anti-PSD-95 (palmitoylated), mAb (rec.) (PF11)...

anti-PSD-95 (palmitoylated), mAb (rec.) (PF11)

PSD-95 is a member of proteins located at a specialized postsynaptic membrane region, called the postsynaptic density (PSD). PSD-95 is the most abundant scaffold protein specifically enriched in the PSD. It contains three PDZ domains, an SH3 domain and a guanylate kinase (GuK)-like domain. Through its PDZ domains, PSD-95 assembles various synaptic components at the PSD including intracellular signaling molecules (e.g. SynGAP and kalirin-7), ion channels (e.g. stargazin/AMPA receptors [AMPARs] and NMDA receptors) and cell adhesion molecules (e.g. neuroligin). PSD-95 plays a primary role in synaptic development and maturation and is regulated by palmitoylation at its N-terminal cysteine residues leading to its postsynaptic targeting. Palmitoylation of PSD-95 is triggered by DHHC2, a plasma membrane-inserted palmitoylating enzyme. Palmitoylated PSD-95 is almost exclusively localized at excitatory synapses in neurons. - Recombinant Antibody. Recognizes human, mouse and rat palmitoylated PSD-95. Isotype: Human IgG2. Clone: PF11. Applications: ICC, IHC. Liquid. In PBS containing 10% glycerol. PSD-95 is a member of proteins located at a specialized postsynaptic membrane region, called the postsynaptic density (PSD). PSD-95 is the most abundant scaffold protein specifically enriched in the PSD. It contains three PDZ domains, an SH3 domain and a guanylate kinase (GuK)-like domain. Through its PDZ domains, PSD-95 assembles various synaptic components at the PSD including intracellular signaling molecules (e.g. SynGAP and kalirin-7), ion channels (e.g. stargazin/AMPA receptors [AMPARs] and NMDA receptors) and cell adhesion molecules (e.g. neuroligin). PSD-95 plays a primary role in synaptic development and maturation and is regulated by palmitoylation at its N-terminal cysteine residues leading to its postsynaptic targeting. Palmitoylation of PSD-95 is triggered by DHHC2, a plasma membrane-inserted palmitoylating enzyme. Palmitoylated PSD-95 is almost exclusively localized at excitatory synapses in neurons.

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